ID X0BDB1_FUSOX Unreviewed; 1436 AA.
AC X0BDB1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=sterol 3beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012650};
DE EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
DE AltName: Full=Autophagy-related protein 26 {ECO:0000256|ARBA:ARBA00029843};
GN ORFNames=FOQG_15627 {ECO:0000313|EMBL:EXK79791.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK79791.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK79791.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK79791.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside +
CC H(+) + UDP; Xref=Rhea:RHEA:22724, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:37424, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; EC=2.4.1.173;
CC Evidence={ECO:0000256|ARBA:ARBA00035583};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22725;
CC Evidence={ECO:0000256|ARBA:ARBA00035583};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ergosterol + UDP-alpha-D-glucose = ergosteryl 3-beta-D-
CC glucoside + H(+) + UDP; Xref=Rhea:RHEA:61836, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16933, ChEBI:CHEBI:52973, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; Evidence={ECO:0000256|ARBA:ARBA00035586};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61837;
CC Evidence={ECO:0000256|ARBA:ARBA00035586};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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DR EMBL; JH658459; EXK79791.1; -; Genomic_DNA.
DR eggNOG; KOG1192; Eukaryota.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102203; F:brassicasterol glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102205; F:cholesterol alpha-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051506; F:ergosterol UDP-glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR CDD; cd13215; PH-GRAM1_AGT26; 1.
DR CDD; cd13216; PH-GRAM2_AGT26; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR InterPro; IPR048066; ATG26_PH_GRAM1.
DR InterPro; IPR048065; ATG26_PH_GRAM2.
DR InterPro; IPR010610; EryCIII-like_C.
DR InterPro; IPR004276; GlycoTrans_28_N.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR002213; UDP_glucos_trans.
DR PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR48050:SF25; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF06722; EryCIII-like_C; 1.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR Pfam; PF02893; GRAM; 2.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXK79791.1}.
FT DOMAIN 282..378
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1436 AA; 160910 MW; 46DEBB1A30A026F8 CRC64;
MASQADDAPA QASIGAGDIK EHVHEELHRR KRQNSTATVF PEPLRESDAE DEEEDDTTQG
PPMFMNMNQS IFGLIATASS RVDFNDRFDG MSSDEEGEGS SSQHSRDHIA QTSILQPGGK
GKDKGHRRKR LSEHKLLRSL PALPKLRSRH KSQPSRLSAP VETADESDVE DNGTLSPAPA
LTLTRQDTQG VMSRMLEAKA DLSSRPSFDL DRLSSDVSRS SDGEVVSALA KKLKEIFEFD
TYEQVIEEYP CWLLQSVLLQ GYMYITSKHI CFYAYLPKKA NEAVKSGYLS KSGKRNPSYT
RFWFRLKGDV LAYYKTATDV YFPHGQIDLR YGISANIVDK DKEGLHFTVE THHRTYKFKA
DSAPSAKEWV KSLQRVIFRS HNDGDSVKIS LPIKNVIDIE DTQMIAFADT CKVRVIDNDE
TYAIDEYFFS FFSFGKDAIN VLKILIEASA ESRSAEKAVS SREENESSQP PSGRTSMAAS
RHLPQIDRLH TGKLPDTVKA TLAPMSPLSP HSPSQLSPRA SMDAPRSSFD GFRRFGRKSM
DVPSSIGDFS PRRSFSGTRR STSRHQHGST TPKQQQAQDS GDSFIHSSID NPSISTLSPS
SFEDPSASQI LQGSEVFHSP TMRRSASASR KRDQSGKKTP RNSTSNRERP RHIHHAATTG
AMQEMGGETS DSQRPVTPTL NSITKIGAYP LQRANAFAEY LSRTSQRMGS MFATESLGYV
EKVHGMWKGE HRHYDEPQEL KTDDDADDID SDAEDKTQTA MDRFRAHFTL PESEKLVATY
FGAIFKVLPL YGKFYISDRS FCFRSLYPGT RTKLILPLKD IENVHKEKGF RFGYYGLTVV
IRGHEELFFE FRRPGLRDDC AVTLHQLMET NRFLEKSGFL DQEEQDDEEA AAAIAERDAL
KAARQDEFVN HELELPRETS GVSNAPTILF DNPNSSGLAF KPQKSMKITC LTIGSRGDVQ
PYIALCKGLL AEGHKPRIAT HAEFQGWIES HGIEFARVEG DPGELMRLCI ENGTFTWAFL
REANSTFRGW LDELLDSAYT ACEGSELLIE SPSAMAGIHI AEKLGIPYFR AFTMPWTRTR
AYPHAFIMPE HKMGGAYNYM TYVMFDNIFW KATAFQVNRW RRKTLGLPST NLEKMQPNKV
PFLYNFSPSV VAPPLDFSDW IRVTGYWFLN EGGDWEPPQE LQDFIAKARA DGKKLVYVGF
GSIIVKDPAK MTQEVIDAVL KADVRCILSK GWSDRISPKD DPSKPRPEEP EMPPEIHVIK
SAPHDWLFSQ IDAAAHHGGS GTTGASLRAG IPTIIRPFFG DQFFFATRVE DLGVGVWVKK
WGTNSFGRAL WEVTRNERMI VKARVLGEQI RSESGVDSAI QCIYRDLEYA KSLIKRNAGK
AAQHDANEDD DTEESWTFVG RDEPDPDAVT KKLSEGLVDT EKPLSLGSQA PSTAAA
//
